Peptide-based coacervates in therapeutic applications

被引:15
作者
Ma, Lilusi [1 ,2 ]
Fang, Xiaocui [1 ,2 ]
Wang, Chen [1 ,2 ]
机构
[1] Natl Ctr Nanosci & Technol, CAS Ctr Excellence Nanosci, CAS Key Lab Biol Effects Nanomat & Nanosafety, CAS Key Lab Standardizat & Measurement Nanotechnol, Beijing, Peoples R China
[2] Univ Chinese Acad Sci, Beijing, Peoples R China
基金
中国国家自然科学基金;
关键词
peptide; coacervate; liquid liquid phase separation; self-assembly; complex assembly; LIQUID PHASE-SEPARATION; COMPLEX COACERVATION; IN-SITU; DELIVERY; PROTEIN; TRANSITION; HYDROGELS; MOLECULE; BINDING; MODEL;
D O I
10.3389/fbioe.2022.1100365
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Coacervates are droplets formed by liquid-liquid phase separation. An increasing number of studies have reported that coacervates play an important role in living cells, such as in the generation of membraneless organelles, and peptides contribute to condensate droplet formation. Peptides with versatile functional groups and special secondary structures, including alpha-helices, beta-sheets and intrinsically disordered regions, provide novel insights into coacervation, such as biomimetic protocells, neurodegenerative diseases, modulations of signal transmission, and drug delivery systems. In this review, we introduce different types of peptide-based coacervates and the principles of their interactions. Additionally, we summarize the thermodynamic and kinetic mechanisms of peptide-based coacervates and the associated factors, including salt, pH, and temperature, affecting the phase separation process. We illustrate recent studies on modulating the functions of peptide-based coacervates applied in biological diseases. Finally, we propose their promising broad applications and describe the challenges of peptide-based coacervates in the future.
引用
收藏
页数:21
相关论文
共 109 条
[1]   Formulation and evaluation of an in situ gel forming system for controlled delivery of triptorelin acetate [J].
Abashzadeh, Sh. ;
Dinarvand, R. ;
Sharifzadeh, M. ;
Hassanzadeh, G. ;
Amini, M. ;
Atyabi, F. .
EUROPEAN JOURNAL OF PHARMACEUTICAL SCIENCES, 2011, 44 (04) :514-521
[2]   Peptide-Based Coacervate-Core Vesicles with Semipermeable Membranes [J].
Abbas, Manzar ;
Law, Jack O. ;
Grellscheid, Sushma N. ;
Huck, Wilhelm T. S. ;
Spruijt, Evan .
ADVANCED MATERIALS, 2022, 34 (34)
[3]   Preparation and characterization of novel elastin-like polypeptide-collagen composites [J].
Amruthwar, Shruti S. ;
Puckett, Aaron D. ;
Janorkar, Amol V. .
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A, 2013, 101 (08) :2383-2391
[4]   RNA-Based Coacervates as a Model for Membraneless Organelles: Formation, Properties, and Interfacial Liposome Assembly [J].
Aumiller, William M., Jr. ;
Cakmak, Fatma Pir ;
Davis, Bradley W. ;
Keating, Christine D. .
LANGMUIR, 2016, 32 (39) :10042-10053
[5]  
Aumiller WM, 2016, NAT CHEM, V8, P129, DOI [10.1038/NCHEM.2414, 10.1038/nchem.2414]
[6]   Liquid-Liquid Phase Separation of Peptide/Oligonucleotide Complexes in Crowded Macromolecular Media [J].
Bai, Qingwen ;
Zhang, Qiufen ;
Jing, Hairong ;
Chen, Jiaxin ;
Liang, Dehai .
JOURNAL OF PHYSICAL CHEMISTRY B, 2021, 125 (01) :49-57
[7]   Fundamental Challenges and Outlook in Simulating Liquid-Liquid Phase Separation of Intrinsically Disordered Proteins [J].
Bari, Khandekar Jishan ;
Prakashchand, Dube Dheeraj .
JOURNAL OF PHYSICAL CHEMISTRY LETTERS, 2021, 12 (06) :1644-1656
[8]   Thermal Compaction of Disordered and Elastin-like Polypeptides: A Temperature-Dependent, Sequence-Specific Coarse-Grained Simulation Model [J].
Baul, Upayan ;
Bley, Michael ;
Dzubiella, Joachim .
BIOMACROMOLECULES, 2020, 21 (09) :3523-3538
[9]   Encapsulating a Hydrophilic Chemotherapeutic into Rod-Like Nanoparticles of a Genetically Encoded Asymmetric Triblock Polypeptide Improves Its Efficacy [J].
Bhattacharyya, Jayanta ;
Weitzhandler, Isaac ;
Ho, Shihan Bryan ;
McDaniel, Jonathan R. ;
Li, Xinghai ;
Tang, Lei ;
Liu, Jinyao ;
Dewhirst, Mark ;
Chilkoti, Ashutosh .
ADVANCED FUNCTIONAL MATERIALS, 2017, 27 (12)
[10]   Granulins modulate liquid?liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43 [J].
Bhopatkar, Anukool A. ;
Uversky, Vladimir N. ;
Rangachari, Vijayaraghavan .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2020, 295 (08) :2506-2519